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Am J Physiol Endocrinol Metab 280: E160-E170, 2001;
0193-1849/01 $5.00
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Vol. 280, Issue 1, E160-E170, January 2001

Regulation of prohormone convertase 1 (PC1) by thyroid hormone

Qiao-Ling Li1,2, Erik Jansen4, Gregory A. Brent3, and Theodore C. Friedman1,2

1 Division of Endocrinology, Department of Medicine, Cedars-Sinai Research Institute- University of California at Los Angeles (UCLA) School of Medicine, Los Angeles 90048; 2 Division of Endocrinology, Charles R. Drew University of Medicine and Sciences- UCLA School of Medicine, Los Angeles 90059; 3 Division of Endocrinology, Department of Medicine, West Los Angeles Veterans Affairs Medical Center, Los Angeles, CA 90073; and 4 Laboratory for Molecular Oncology, Center for Human Genetics, University of Leuven and the Flanders Interuniversity Institute for Biotechnology, B-3000 Leuven, Belgium

The prohormone convertases (PCs) PC1 and PC2 are key enzymes capable of processing a variety of prohormones to their bioactive forms. In this study, we demonstrated that 6-n-propyl-2-thiouracil (PTU)-induced hypothyroidism stimulated, whereas triido-L-thyronine (T3)-induced hyperthyroidism suppressed, PC1 mRNA levels in the rat anterior pituitary. Using 5' deletions of the human PC1 (hPC1) promoter transiently transfected into GH3 (a somatotroph cell line) cells, we found that T3 negatively regulated hPC1 promoter activity and that this regulation required the region from -82 to +19 bp relative to the transcription start site. Electrophoretic mobility shift assays (EMSAs) using purified thyroid hormone receptor-alpha 1 (TRalpha 1) and retinoid X receptor-beta (RXRbeta ) proteins and GH3 nuclear extracts demonstrated that the region from -10 to +19 bp of the hPC1 promoter bound TRalpha 1 as both a monomer and a homodimer and bound TRalpha 1/RXRbeta as a heterodimer and multimer. EMSAs with oligonucleotides containing point mutations of the putative negative thyroid response elements (TREs) exhibited diminished homodimer and loss of multimer binding. We conclude that there are multiple novel TRE-like sequences in the hPC1 promoter located from -10 to +19 bp.

posttranslational processing; negative thyroid response element; hypothyroidism; processing enzyme; pituitary; regulation; triiodo-L-thyronine


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